3P48
Structure of the yeast dUTPase DUT1 in complex with dUMPNPP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004170 | molecular_function | dUTP diphosphatase activity |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006226 | biological_process | dUMP biosynthetic process |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0009213 | biological_process | pyrimidine deoxyribonucleoside triphosphate catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0035863 | biological_process | dITP catabolic process |
A | 0035870 | molecular_function | dITP diphosphatase activity |
A | 0046081 | biological_process | dUTP catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004170 | molecular_function | dUTP diphosphatase activity |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0006226 | biological_process | dUMP biosynthetic process |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0009213 | biological_process | pyrimidine deoxyribonucleoside triphosphate catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0035863 | biological_process | dITP catabolic process |
B | 0035870 | molecular_function | dITP diphosphatase activity |
B | 0046081 | biological_process | dUTP catabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004170 | molecular_function | dUTP diphosphatase activity |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0006226 | biological_process | dUMP biosynthetic process |
C | 0009117 | biological_process | nucleotide metabolic process |
C | 0009213 | biological_process | pyrimidine deoxyribonucleoside triphosphate catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0035863 | biological_process | dITP catabolic process |
C | 0035870 | molecular_function | dITP diphosphatase activity |
C | 0046081 | biological_process | dUTP catabolic process |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE DUP A 148 |
Chain | Residue |
A | ARG68 |
A | HOH186 |
A | HOH211 |
A | HOH246 |
A | HOH247 |
A | HOH260 |
A | HOH406 |
C | LYS74 |
C | ALA81 |
C | GLY82 |
C | VAL83 |
A | SER69 |
C | ASP85 |
C | TYR88 |
C | LYS93 |
A | GLY70 |
A | GLN114 |
A | MG149 |
A | HOH164 |
A | HOH168 |
A | HOH176 |
A | HOH178 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 149 |
Chain | Residue |
A | DUP148 |
A | HOH168 |
A | HOH246 |
A | HOH247 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE DUP B 148 |
Chain | Residue |
A | ALA81 |
A | GLY82 |
A | VAL83 |
A | ASP85 |
A | TYR88 |
A | VAL92 |
A | LYS93 |
B | ARG68 |
B | SER69 |
B | GLY70 |
B | GLN114 |
B | MG150 |
B | HOH161 |
B | HOH175 |
B | HOH180 |
B | HOH207 |
B | HOH214 |
B | HOH219 |
B | HOH248 |
B | HOH249 |
B | HOH250 |
B | HOH257 |
B | HOH396 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE DUP B 149 |
Chain | Residue |
B | ALA81 |
B | GLY82 |
B | VAL83 |
B | ASP85 |
B | TYR88 |
B | VAL92 |
B | LYS93 |
B | HOH190 |
B | HOH225 |
B | HOH234 |
B | HOH276 |
B | HOH377 |
C | MET48 |
C | ARG68 |
C | SER69 |
C | GLY70 |
C | GLN114 |
C | MG148 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 150 |
Chain | Residue |
B | DUP148 |
B | HOH248 |
B | HOH249 |
B | HOH250 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 148 |
Chain | Residue |
B | DUP149 |
B | HOH276 |
C | ASP32 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21548881, ECO:0007744|PDB:3F4F |
Chain | Residue | Details |
A | SER69 | |
B | GLY82 | |
B | ASP85 | |
B | TYR88 | |
B | LYS93 | |
B | ARG137 | |
B | PHE142 | |
B | GLY143 | |
C | SER69 | |
C | GLY82 | |
C | ASP85 | |
A | GLY82 | |
C | TYR88 | |
C | LYS93 | |
C | ARG137 | |
C | PHE142 | |
C | GLY143 | |
A | ASP85 | |
A | TYR88 | |
A | LYS93 | |
A | ARG137 | |
A | PHE142 | |
A | GLY143 | |
B | SER69 |